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Protein

Heat shock 70 kDa protein 6

Gene

HSPA6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei73 – 731ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 174ATP
Nucleotide bindingi204 – 2063ATP
Nucleotide bindingi270 – 2778ATP
Nucleotide bindingi341 – 3444ATP

GO - Molecular functioni

  • ATPase activity, coupled Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • cellular response to heat Source: UniProtKB
  • protein refolding Source: UniProtKB
  • response to unfolded protein Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 6
Alternative name(s):
Heat shock 70 kDa protein B'
Gene namesi
Name:HSPA6
Synonyms:HSP70B'
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:5239. HSPA6.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • centriole Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi563 – 5631K → R: Complete loss of in vitro methylation by METTL21A. 1 Publication

Organism-specific databases

PharmGKBiPA29505.

Chemistry

ChEMBLiCHEMBL3232688.

Polymorphism and mutation databases

BioMutaiHSPA6.
DMDMi34978357.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 643643Heat shock 70 kDa protein 6PRO_0000078264Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysineBy similarity
Modified residuei136 – 1361Nitrated tyrosineBy similarity
Modified residuei330 – 3301N6-acetyllysine; alternateBy similarity
Cross-linki330 – 330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei497 – 4971PhosphothreonineBy similarity
Modified residuei563 – 5631N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication
Modified residuei626 – 6261PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Nitration, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP17066.
MaxQBiP17066.
PaxDbiP17066.
PeptideAtlasiP17066.
PRIDEiP17066.

2D gel databases

UCD-2DPAGEP17066.

PTM databases

iPTMnetiP17066.
PhosphoSiteiP17066.
SwissPalmiP17066.

Expressioni

Inductioni

Only at higher temperatures, and no basal expression.

Gene expression databases

BgeeiP17066.
CleanExiHS_HSPA6.
GenevisibleiP17066. HS.

Organism-specific databases

HPAiCAB017452.
HPA028549.
HPA052504.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TERF1P542742EBI-355106,EBI-710997

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • heat shock protein binding Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109542. 78 interactions.
IntActiP17066. 35 interactions.
MINTiMINT-1139180.
STRINGi9606.ENSP00000310219.

Structurei

Secondary structure

1
643
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 124Combined sources
Beta strandi15 – 2410Combined sources
Beta strandi27 – 304Combined sources
Beta strandi38 – 414Combined sources
Beta strandi44 – 463Combined sources
Beta strandi51 – 533Combined sources
Helixi55 – 595Combined sources
Turni60 – 634Combined sources
Helixi65 – 673Combined sources
Helixi72 – 743Combined sources
Turni75 – 773Combined sources
Helixi83 – 908Combined sources
Beta strandi93 – 997Combined sources
Beta strandi102 – 1098Combined sources
Beta strandi112 – 1165Combined sources
Helixi118 – 13720Combined sources
Beta strandi143 – 1486Combined sources
Helixi154 – 16613Combined sources
Beta strandi170 – 1767Combined sources
Helixi177 – 1848Combined sources
Turni185 – 1884Combined sources
Beta strandi195 – 2028Combined sources
Beta strandi207 – 2159Combined sources
Beta strandi218 – 22710Combined sources
Helixi232 – 25120Combined sources
Helixi259 – 27517Combined sources
Turni276 – 2783Combined sources
Beta strandi280 – 29011Combined sources
Beta strandi293 – 3008Combined sources
Helixi301 – 31414Combined sources
Helixi316 – 32611Combined sources
Helixi330 – 3323Combined sources
Beta strandi334 – 3407Combined sources
Helixi341 – 3444Combined sources
Helixi346 – 35510Combined sources
Turni356 – 3583Combined sources
Turni367 – 3693Combined sources
Helixi370 – 38314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE1X-ray2.20A/B/C6-385[»]
ProteinModelPortaliP17066.
SMRiP17066. Positions 6-615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17066.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17066.
KOiK03283.
OMAiICRPIFS.
OrthoDBiEOG7PCJGF.
PhylomeDBiP17066.
TreeFamiTF105042.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P17066-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQAPRELAVG IDLGTTYSCV GVFQQGRVEI LANDQGNRTT PSYVAFTDTE
60 70 80 90 100
RLVGDAAKSQ AALNPHNTVF DAKRLIGRKF ADTTVQSDMK HWPFRVVSEG
110 120 130 140 150
GKPKVRVCYR GEDKTFYPEE ISSMVLSKMK ETAEAYLGQP VKHAVITVPA
160 170 180 190 200
YFNDSQRQAT KDAGAIAGLN VLRIINEPTA AAIAYGLDRR GAGERNVLIF
210 220 230 240 250
DLGGGTFDVS VLSIDAGVFE VKATAGDTHL GGEDFDNRLV NHFMEEFRRK
260 270 280 290 300
HGKDLSGNKR ALRRLRTACE RAKRTLSSST QATLEIDSLF EGVDFYTSIT
310 320 330 340 350
RARFEELCSD LFRSTLEPVE KALRDAKLDK AQIHDVVLVG GSTRIPKVQK
360 370 380 390 400
LLQDFFNGKE LNKSINPDEA VAYGAAVQAA VLMGDKCEKV QDLLLLDVAP
410 420 430 440 450
LSLGLETAGG VMTTLIQRNA TIPTKQTQTF TTYSDNQPGV FIQVYEGERA
460 470 480 490 500
MTKDNNLLGR FELSGIPPAP RGVPQIEVTF DIDANGILSV TATDRSTGKA
510 520 530 540 550
NKITITNDKG RLSKEEVERM VHEAEQYKAE DEAQRDRVAA KNSLEAHVFH
560 570 580 590 600
VKGSLQEESL RDKIPEEDRR KMQDKCREVL AWLEHNQLAE KEEYEHQKRE
610 620 630 640
LEQICRPIFS RLYGGPGVPG GSSCGTQARQ GDPSTGPIIE EVD
Length:643
Mass (Da):71,028
Last modified:September 19, 2003 - v2
Checksum:iBCE348F0226DB70B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 1083RVC → PVS in CAA36061 (PubMed:2327978).Curated
Sequence conflicti263 – 2631R → G in CAA36061 (PubMed:2327978).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti65 – 651P → T.1 Publication
Corresponds to variant rs549201566 [ dbSNP | Ensembl ].
VAR_060718
Natural varianti95 – 951R → Q.1 Publication
Corresponds to variant rs400835 [ dbSNP | Ensembl ].
VAR_060719
Natural varianti150 – 1501A → T.1 Publication
Corresponds to variant rs10919224 [ dbSNP | Ensembl ].
VAR_049605
Natural varianti153 – 1531N → S.1 Publication
Corresponds to variant rs10919225 [ dbSNP | Ensembl ].
VAR_049606
Natural varianti154 – 1541D → N.1 Publication
Corresponds to variant rs10919226 [ dbSNP | Ensembl ].
VAR_049607
Natural varianti159 – 1591A → V.1 Publication
Corresponds to variant rs41297702 [ dbSNP | Ensembl ].
VAR_060720
Natural varianti170 – 1701N → K.1 Publication
Corresponds to variant rs41297704 [ dbSNP | Ensembl ].
VAR_049608
Natural varianti173 – 1731R → P.1 Publication
Corresponds to variant rs41297708 [ dbSNP | Ensembl ].
VAR_049609
Natural varianti178 – 1781P → A.1 Publication
Corresponds to variant rs41297710 [ dbSNP | Ensembl ].
VAR_049610
Natural varianti194 – 1941E → K.1 Publication
Corresponds to variant rs41297714 [ dbSNP | Ensembl ].
VAR_049611
Natural varianti198 – 1981L → F.1 Publication
Corresponds to variant rs63749092 [ dbSNP | Ensembl ].
VAR_024182
Natural varianti260 – 2601R → H.
Corresponds to variant rs41299256 [ dbSNP | Ensembl ].
VAR_049612
Natural varianti297 – 2971T → K.1 Publication
Corresponds to variant rs41297718 [ dbSNP | Ensembl ].
VAR_060721
Natural varianti336 – 3361V → F.
Corresponds to variant rs417707 [ dbSNP | Ensembl ].
VAR_059360
Natural varianti464 – 4641S → I.1 Publication
Corresponds to variant rs388218 [ dbSNP | Ensembl ].
VAR_049613
Natural varianti471 – 4711R → H.1 Publication
Corresponds to variant rs41299256 [ dbSNP | Ensembl ].
VAR_049614
Natural varianti528 – 5281K → E.1 Publication
Corresponds to variant rs570189 [ dbSNP | Ensembl ].
VAR_049615
Natural varianti528 – 5281K → R.
Corresponds to variant rs570167 [ dbSNP | Ensembl ].
VAR_059361
Natural varianti562 – 5621D → E.1 Publication
Corresponds to variant rs753856 [ dbSNP | Ensembl ].
VAR_024183
Natural varianti572 – 5721M → V.
Corresponds to variant rs452004 [ dbSNP | Ensembl ].
VAR_049616
Natural varianti577 – 5771R → Q.1 Publication
Corresponds to variant rs368844 [ dbSNP | Ensembl ].
VAR_049617
Natural varianti626 – 6261T → A.1 Publication
Corresponds to variant rs41299260 [ dbSNP | Ensembl ].
VAR_049618

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.
CCDSiCCDS1231.1.
PIRiS09036.
RefSeqiNP_002146.2. NM_002155.4.
UniGeneiHs.654614.

Genome annotation databases

EnsembliENST00000309758; ENSP00000310219; ENSG00000173110.
GeneIDi3310.
KEGGihsa:3310.
UCSCiuc001gaq.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51757 Genomic DNA. Translation: CAA36061.1.
X51758 mRNA. Translation: CAA36062.1.
DQ521571 Genomic DNA. Translation: ABF47108.1.
AL590385 Genomic DNA. Translation: CAI16120.1.
BC004279 mRNA. Translation: AAH04279.1.
BC035665 mRNA. Translation: AAH35665.1.
S78631 Genomic DNA. No translation available.
CCDSiCCDS1231.1.
PIRiS09036.
RefSeqiNP_002146.2. NM_002155.4.
UniGeneiHs.654614.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3FE1X-ray2.20A/B/C6-385[»]
ProteinModelPortaliP17066.
SMRiP17066. Positions 6-615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109542. 78 interactions.
IntActiP17066. 35 interactions.
MINTiMINT-1139180.
STRINGi9606.ENSP00000310219.

Chemistry

ChEMBLiCHEMBL3232688.

PTM databases

iPTMnetiP17066.
PhosphoSiteiP17066.
SwissPalmiP17066.

Polymorphism and mutation databases

BioMutaiHSPA6.
DMDMi34978357.

2D gel databases

UCD-2DPAGEP17066.

Proteomic databases

EPDiP17066.
MaxQBiP17066.
PaxDbiP17066.
PeptideAtlasiP17066.
PRIDEiP17066.

Protocols and materials databases

DNASUi3310.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309758; ENSP00000310219; ENSG00000173110.
GeneIDi3310.
KEGGihsa:3310.
UCSCiuc001gaq.4. human.

Organism-specific databases

CTDi3310.
GeneCardsiHSPA6.
HGNCiHGNC:5239. HSPA6.
HPAiCAB017452.
HPA028549.
HPA052504.
MIMi140555. gene.
neXtProtiNX_P17066.
PharmGKBiPA29505.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17066.
KOiK03283.
OMAiICRPIFS.
OrthoDBiEOG7PCJGF.
PhylomeDBiP17066.
TreeFamiTF105042.

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

EvolutionaryTraceiP17066.
GeneWikiiHSPA6.
GenomeRNAii3310.
PROiP17066.
SOURCEiSearch...

Gene expression databases

BgeeiP17066.
CleanExiHS_HSPA6.
GenevisibleiP17066. HS.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human heat-shock protein family. Expression of a novel heat-inducible HSP70 (HSP70B') and isolation of its cDNA and genomic DNA."
    Leung T.K.C., Rajendran M.Y., Monfries C., Hall C., Lim L.
    Biochem. J. 267:125-132(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Lung.
  2. NIEHS SNPs program
    Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-65; GLN-95; THR-150; SER-153; ASN-154; VAL-159; LYS-170; PRO-173; ALA-178; LYS-194; PHE-198; LYS-297; ILE-464; HIS-471; GLU-528; GLU-562; GLN-577 AND ALA-626.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary and Skin.
  5. "The human heat-shock genes HSPA6 and HSPA7 are both expressed and localize to chromosome 1."
    Leung T.K.C., Hall C., Rajendran M., Spurr N.K., Lim L.
    Genomics 12:74-79(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-250.
  6. "Cis-acting elements involved in the regulated expression of a human HSP70 gene."
    Schiller P., Amin J., Ananthan J., Brown M.E., Scott W.A., Voellmy R.
    J. Mol. Biol. 203:97-105(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
  7. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-563, MUTAGENESIS OF LYS-563.
  8. "Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
    Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
    PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 6-385 IN COMPLEX WITH ADP AND PHOSPHATE.

Entry informationi

Entry nameiHSP76_HUMAN
AccessioniPrimary (citable) accession number: P17066
Secondary accession number(s): Q1HBA8, Q8IYK7, Q9BT95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: September 19, 2003
Last modified: July 6, 2016
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.